SHIP1 and Lyn Kinase Negatively Regulate Integrin αIIbβ3 Signaling in Platelets
作者： Mhairi J. Maxwell , Yuping Yuan , Karen E. Anderson , Margaret L. Hibbs , Hatem H. Salem
关键词:
摘要: Integrin αIIbβ3 plays a critical role in platelet function, promoting broad range of functional responses including adhesion, spreading, aggregation, clot retraction, and procoagulant function. Signaling events operating downstream this receptor (outside-in signaling) are important for these responses; however the mechanisms negatively regulating integrin signaling remain ill-defined. We demonstrate here major Src homology 2 domain-containing inositol 5-phosphatase (SHIP1) family kinase, Lyn, process. Our studies on murine SHIP1 knockout platelets have defined enzyme αIIbβ3-dependent phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) accumulation, necessary cytosolic calcium response spreading. phosphorylation PtdIns(3,4,5)P3 metabolism is partially regulated through Lyn resulting an enhanced flux spreading Lyn-deficient mouse platelets. Analysis adhesion dynamics under physiological blood flow conditions revealed fibrinogen. Specifically, SHIP1-dependent down-regulates stability αIIbβ3-fibrinogen adhesive bonds, leading to decrease proportion forming shear-resistant contacts. These define as negative regulators
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